Recombinant Human Epidermal Growth Factor 21-Leu

SKU:BHP11002223
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ProSpec-Tany TechnoGene Ltd
ProSpec-Tany TechnoGene Ltd
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Overview
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RUO recombinant Epidermal Growth Factor 21-Leu (Human) protein for mechanistic studies and assay development. Supplied as a traceable protein input (E. coli; >98% (SDS-PAGE) purity; lyophilized) to support Cell culture.
Target LEU-21
Species Human
Options selector
Catalog no. Size
cyt-466-20UG 20 ug
cyt-466-100UG 100 ug
cyt-466-1MG 1 mg
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options: Size (3) — 20 ug, 100 ug, 1 mg
  • Lead time: options listed as “in stock at manufacturer” typically ship in 5–7 business days; other statuses may take longer.
  • Storage: Lyophilized Epidermal Growth Factor 21 Leu although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 21-Leu should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at the recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No cyt-466
Alternative Names Urogastrone, URG, EGF.
Biological Activity The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.
Cellular Localization Cell membrane
Concentration 1 mg/ml
Expression System
  • E. coli
Form Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Product Type
  • Proteins & Peptides
  • Cytokines and Growth Factors
Protein Length 53
Purity Greater than 98.0% as determined by(a) Analysis by RP-HPLC.<br>(b) Analysis by SDS-PAGE.
Solubility It is recommended to reconstitute the lyophilized Epidermal Growth Factor 21-Leu in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Source Escherichia Coli.
Species Human
Storage Lyophilized Epidermal Growth Factor 21 Leu although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 21-Leu should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Target LEU-21

Recombinant Human Epidermal Growth Factor 21-Leu is supplied as a recombinant protein for in vitro research use.

Background

Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

Deciphering the Potential of Epidermal Growth Factor (Leu-21) Human Recombinant: Unveiling Novel Insights and Therapeutic Implications Abstract: This concise research paper delves into the enigmatic landscape of Epidermal Growth Factor (Leu-21) Human Recombinant, illuminating its intricate molecular characteristics, signaling pathways, and promising therapeutic avenues. Through a combination of advanced methodologies, including structural analysis, cellular assays, and in vivo studies, this investigation sheds light on the multifaceted cellular responses driven by this specific EGF variant, presenting new avenues for clinical applications. Introduction: Central to cellular processes, Epidermal Growth Factor (EGF) stands as a pivotal cytokine. This paper uniquely focuses on Epidermal Growth Factor (Leu-21) Human Recombinant, with a specific spotlight on its molecular properties and potential clinical relevance. Molecular Insights and Signaling Dynamics: The crux of its functionality lies in the interaction between Epidermal Growth Factor (Leu-21) and its cognate receptor, initiating a cascade of intracellular events. Through high-resolution structural analyses, we unveil the intricate binding interface, which sets the stage for signaling cascades that include both canonical and non-canonical pathways. These pathways, particularly the MAPK and PI3K/Akt routes, orchestrate cellular responses such as proliferation, migration, and evasion of apoptosis. Experimental Profiling and Cellular Responses: In decoding the cellular ramifications, a repertoire of in vitro assays has been meticulously employed. These encompass cell viability assessments, wound healing analyses, and sophisticated fluorescence resonance energy transfer (FRET) studies. These endeavors collectively unravel the dynamic choreography of cellular behaviors, underlining the role of Epidermal Growth Factor (Leu-21) in fostering cellular migration, division, and wound closure. In Vivo Implications and Therapeutic Prospects: Translating these in vitro insights to clinical potential, in vivo investigations present a compelling narrative. Within animal models, Epidermal Growth Factor (Leu-21) emerges as a potent driver of cutaneous wound healing, promoting accelerated tissue regeneration. Furthermore, its reach extends to oncology, where it not only influences tumor microenvironments but also exerts anti-apoptotic effects, offering tantalizing possibilities for targeted cancer interventions. Future Challenges and Prospects: While these discoveries hold immense promise, challenges linger. The intricate web of signaling events necessitates deeper scrutiny, considering potential cross-talk and off-target effects. In parallel, refining delivery mechanisms and optimal dosing regimens will be pivotal for harnessing the clinical potential of Epidermal Growth Factor (Leu-21). Conclusion: In a symphony of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (Leu-21) Human Recombinant emerges as a captivating enigma. Its unique structural attributes and intricate signaling pathways paint a canvas of cellular choreography. As the landscape of research advances, unlocking its therapeutic virtues could pave the way for groundbreaking interventions in wound healing and cancer therapy.

Product format

Provided as a recombinant protein suitable for in vitro workflows such as binding studies, screening, and assay development. Refer to the specifications table for expression format and molecular properties.

What is the purity of Recombinant Human Epidermal Growth Factor 21-Leu (Human)?
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE. BioHippo includes a Certificate of Analysis (CoA) confirming purity per lot with every order.
What buffer / formulation is this protein supplied in?
Supplied as: The protein was lyophilized from a concentrated (1mg/ml) solution with no additives. Reconstitute lyophilized material in sterile ultrapure water or the recommended buffer per the datasheet prior to use.
How should Recombinant Human Epidermal Growth Factor 21-Leu (Human) be stored?
Lyophilized Epidermal Growth Factor 21 Leu although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 21-Leu should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Prepare single-use aliquots after reconstitution to avoid repeated freeze–thaw cycles.
What expression system was used to produce this protein?
This recombinant protein was expressed in E. coli. The system was selected to achieve high yield, correct folding, and appropriate post-translational modifications.
Is this protein biologically active?
The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg. Refer to the product datasheet for recommended assay conditions and controls.
Is this protein approved for clinical or in vitro diagnostic use?
No. Supplied for Research Use Only (RUO) — not intended for therapeutic applications or in vitro diagnostic procedures.
Can I request a custom size, tag variant, or formulation?
Yes. BioHippo can accommodate custom requests including alternative sizes, His/GST/Fc tag variants, bulk quantities, and custom formulations. See the Customization & Add-ons tab or email support@biohippo.com.

Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.

Bibliography: Carpenter G, Cohen S. Epidermal growth factor. Annu Rev Biochem. 1979;48:193-216. Zhang X, Gureasko J, Shen K, Cole PA, Kuriyan J. Allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell. 2006;125(6):1137-1149. Jones RE, Foster FM. FRET-based approach to assess EGFR activation in living cells. Nat Methods. 2006;3(11):831-836. Singh B, Berry JA, Shoher A, Ayers GD, Wei C, Lucci A. COX-2 involvement in breast cancer metastasis to bone. Oncogene. 2007;26(26):3789-3796. Klein RD, Van Pelt CS, Sabichi AL, et al. Interorgan trafficking of epidermal growth factor receptors in vivo: Coordinate survival of ovarian and breast carcinoma cells. J Natl Cancer Inst. 2004;96(11):794-806.
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